Protein phosphatase 1 in association with Bud14 inhibits mitotic exit in Saccharomyces cerevisiae

Mitotic exit in budding yeast is dependent on correct orientation of the mitotic spindle along the cell polarity axis. When accurate positioning of the spindle fails, a surveillance mechanism named the spindle position checkpoint (SPOC) prevents cells from exiting mitosis. Mutants with a defective S...

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Autores principales:	Dilara Kocakaplan, Hüseyin Karabürk, Cansu Dilege, Idil Kirdök, Seyma Nur Bektas, Ayse Koca Caydasi
Formato:	article
Lenguaje:	EN
Publicado:	eLife Sciences Publications Ltd 2021
Materias:	cell cycle spindle position checkpoint PP1 signalling mitotic exit Medicine R Science Q Biology (General) QH301-705.5
Acceso en línea:	https://doaj.org/article/3b21a37de7764c95a7c54554b4c3589a
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spelling	oai:doaj.org-article:3b21a37de7764c95a7c54554b4c3589a2021-11-09T14:19:06ZProtein phosphatase 1 in association with Bud14 inhibits mitotic exit in Saccharomyces cerevisiae10.7554/eLife.728332050-084Xe72833https://doaj.org/article/3b21a37de7764c95a7c54554b4c3589a2021-10-01T00:00:00Zhttps://elifesciences.org/articles/72833https://doaj.org/toc/2050-084XMitotic exit in budding yeast is dependent on correct orientation of the mitotic spindle along the cell polarity axis. When accurate positioning of the spindle fails, a surveillance mechanism named the spindle position checkpoint (SPOC) prevents cells from exiting mitosis. Mutants with a defective SPOC become multinucleated and lose their genomic integrity. Yet, a comprehensive understanding of the SPOC mechanism is missing. In this study, we identified the type 1 protein phosphatase, Glc7, in association with its regulatory protein Bud14 as a novel checkpoint component. We further showed that Glc7-Bud14 promotes dephosphorylation of the SPOC effector protein Bfa1. Our results suggest a model in which two mechanisms act in parallel for a robust checkpoint response: first, the SPOC kinase Kin4 isolates Bfa1 away from the inhibitory kinase Cdc5, and second, Glc7-Bud14 dephosphorylates Bfa1 to fully activate the checkpoint effector.Dilara KocakaplanHüseyin KarabürkCansu DilegeIdil KirdökSeyma Nur BektasAyse Koca CaydasieLife Sciences Publications Ltdarticlecell cyclespindle position checkpointPP1signallingmitotic exitMedicineRScienceQBiology (General)QH301-705.5ENeLife, Vol 10 (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	cell cycle spindle position checkpoint PP1 signalling mitotic exit Medicine R Science Q Biology (General) QH301-705.5
spellingShingle	cell cycle spindle position checkpoint PP1 signalling mitotic exit Medicine R Science Q Biology (General) QH301-705.5 Dilara Kocakaplan Hüseyin Karabürk Cansu Dilege Idil Kirdök Seyma Nur Bektas Ayse Koca Caydasi Protein phosphatase 1 in association with Bud14 inhibits mitotic exit in Saccharomyces cerevisiae
description	Mitotic exit in budding yeast is dependent on correct orientation of the mitotic spindle along the cell polarity axis. When accurate positioning of the spindle fails, a surveillance mechanism named the spindle position checkpoint (SPOC) prevents cells from exiting mitosis. Mutants with a defective SPOC become multinucleated and lose their genomic integrity. Yet, a comprehensive understanding of the SPOC mechanism is missing. In this study, we identified the type 1 protein phosphatase, Glc7, in association with its regulatory protein Bud14 as a novel checkpoint component. We further showed that Glc7-Bud14 promotes dephosphorylation of the SPOC effector protein Bfa1. Our results suggest a model in which two mechanisms act in parallel for a robust checkpoint response: first, the SPOC kinase Kin4 isolates Bfa1 away from the inhibitory kinase Cdc5, and second, Glc7-Bud14 dephosphorylates Bfa1 to fully activate the checkpoint effector.
format	article
author	Dilara Kocakaplan Hüseyin Karabürk Cansu Dilege Idil Kirdök Seyma Nur Bektas Ayse Koca Caydasi
author_facet	Dilara Kocakaplan Hüseyin Karabürk Cansu Dilege Idil Kirdök Seyma Nur Bektas Ayse Koca Caydasi
author_sort	Dilara Kocakaplan
title	Protein phosphatase 1 in association with Bud14 inhibits mitotic exit in Saccharomyces cerevisiae
title_short	Protein phosphatase 1 in association with Bud14 inhibits mitotic exit in Saccharomyces cerevisiae
title_full	Protein phosphatase 1 in association with Bud14 inhibits mitotic exit in Saccharomyces cerevisiae
title_fullStr	Protein phosphatase 1 in association with Bud14 inhibits mitotic exit in Saccharomyces cerevisiae
title_full_unstemmed	Protein phosphatase 1 in association with Bud14 inhibits mitotic exit in Saccharomyces cerevisiae
title_sort	protein phosphatase 1 in association with bud14 inhibits mitotic exit in saccharomyces cerevisiae
publisher	eLife Sciences Publications Ltd
publishDate	2021
url	https://doaj.org/article/3b21a37de7764c95a7c54554b4c3589a
work_keys_str_mv	AT dilarakocakaplan proteinphosphatase1inassociationwithbud14inhibitsmitoticexitinsaccharomycescerevisiae AT huseyinkaraburk proteinphosphatase1inassociationwithbud14inhibitsmitoticexitinsaccharomycescerevisiae AT cansudilege proteinphosphatase1inassociationwithbud14inhibitsmitoticexitinsaccharomycescerevisiae AT idilkirdok proteinphosphatase1inassociationwithbud14inhibitsmitoticexitinsaccharomycescerevisiae AT seymanurbektas proteinphosphatase1inassociationwithbud14inhibitsmitoticexitinsaccharomycescerevisiae AT aysekocacaydasi proteinphosphatase1inassociationwithbud14inhibitsmitoticexitinsaccharomycescerevisiae
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Protein phosphatase 1 in association with Bud14 inhibits mitotic exit in Saccharomyces cerevisiae

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